Optimization of the Extraction and Stability of Antioxidative Peptides from Mackerel (Pneumatophorus japonicus) Protein

This study optimizes the preparation conditions for mackerel protein hydrolysate (MPH) by response surface methodology (RSM) and investigates the stability of the antioxidant activity of MPHs (<2.5 kDa). The optimal conditions were as follows: enzyme concentration of 1726.85U/g, pH of 7.00, temperature of 39.55 degrees C, time of 5.5 h, and water/material ratio of 25 : 1, and the maximum DPPH scavenging activity was 79.14%. The MPHs indicated significant cellular antioxidant activity at low concentrations. Furthermore, the temperature and freeze-thaw cycles had little effect on the antioxidative stability while pH had significant effect on the antioxidative stability. In addition, the MPHs were sensitive to the metal ions, such as Fe2+, Fe3+, Zn2+, and Cu2+. Notably, when the concentrations of Fe2+ and Fe3+ were 5mM, the DPPH scavenging activities were only 1.1% and 0.6%, respectively; furthermore, Cu2+ at a 5mM concentration could completely inhibit the DPPH scavenging activity of MPHs. In contrast, K+ and Mg2+ had no notable effect on the antioxidant activity of MPHs. These results may provide a scientific basis for the processing and application of MPHs.